ReviewBiochimica et biophysica acta2014
Pyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion tool.
Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 230 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
230 citing papers in PubMed, 403 citations in OpenAlex.
- Eukaryotic cell-free protein synthesis: Chassis diversification, system engineering, and emerging applications.Synthetic and systems biotechnology · 2026Review
- Automated prototyping of genetic codes.Nature · 2026Article
- Cold Orthogonal Translation: A Psychrophilic Pyrrolysyl-tRNA Synthetase Boosts Genetic Code Expansion in E. coli.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Site-Specific Antigen Immobilization Improves Autoantibody Binding Efficiency on the Luminex Platform.ACS omega · 2026Article
- Noncanonical amino acids enable plug and play vaccine platform in the ALiCE cell free system.NPJ vaccines · 2026Article
- Expanding the Genetic Code with Lysine Aminoacylation.Journal of the American Chemical Society · 2026Article
- ChIP happens: from biochemical origins to the modern omics toolbox for understanding steroid hormone receptors.The Biochemical journal · 2026Review
- Genetically encoded green-light-responsive photocaged lysine for sequential control of protein function.Chemical science · 2026Article
- Incorporation of Butyryl-Lysine into Phage-Displayed Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Expanding the genetic code: phage-driven evolution of pyrrolysyl-synthetase for site-specific incorporation of synthetic phenylalanine and tyrosine derivatives.Frontiers in molecular biosciences · 2026Article
- Correlating membrane-protein dynamics with function: Integrating bioinformatics, molecular dynamics, and single-molecule FRET.Protein science : a publication of the Protein Society · 2025Article
- Engineered orthogonal translation systems from metagenomic libraries expand the genetic code.bioRxiv : the preprint server for biology · 2025Article
- Engineering unnatural cells with a 21st amino acid as a living epigenetic sensor.Nature communications · 2025Article
- A chemical epigenetic tool to probe site-specific DNA-binding protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Site-selective protein editing by backbone extension acyl rearrangements.Nature chemical biology · 2025Article
- Copper-catalysed azide-alkyne cycloaddition on live M13 bacteriophage for expanding the molecular diversity of phage-displayed peptide libraries.RSC chemical biology · 2025Article
- Machine learning-guided evolution of pyrrolysyl-tRNA synthetase for improved incorporation efficiency of diverse noncanonical amino acids.Nature communications · 2025Article
- Article
- Optimized Directed Evolution of E. coli leucyl-tRNA Synthetase adds many Noncanonical Amino Acids into the Eukaryotic Genetic Code Including Ornithine and NAngewandte Chemie (International ed. in English) · 2025Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
170 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The genetic incorporation of the 22nd proteinogenic amino acid, pyrrolysine (Pyl) at amber codon is achieved by the action of pyrrolysyl-tRNA synthetase (PylRS) together with its cognate tRNA(Pyl). Unlike most aminoacyl-tRNA synthetases, PylRS displays high substrate side chain promiscuity, low selectivity toward its substrate α-amine, and low selectivity toward the anticodon of tRNA(Pyl). These unique but ordinary features of PylRS as an aminoacyl-tRNA synthetase allow the Pyl incorporation machinery to be easily engineered for the genetic incorporation of more than 100 non-canonical amino acids (NCAAs) or α-hydroxy acids into proteins at amber codon and the reassignment of other codons such as ochre UAA, opal UGA, and four-base AGGA codons to code NCAAs.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.